Effects of wheat structure and viscosity on coccidiosis in broiler chickens

In an experiment with broiler chickens to investigate the effects of physical form of wheat and viscosity of digesta on an Eimeria acervulina infection given on day 21, balanced feeds containing 400 g whole wheat/kg (WW) were compared with those with 400 g ground wheat/kg (GW), with or without addition of carboxymethyl cellulose (CMC- vs. CMC ). Neither treatment significantly affected healthy bird performance from days 15 to 21, or bird performance during recovery from the infection, from days 29 to 42. Neither treatment significantly affected total faecal oocyst yields. During the acute phase of the infection (days 22–28), birds fed on WW had significantly lower weight gains (WW=39.2 g per day, GW=51.8 g per day) and lower food conversion efficiency (FCE; GW=0.50; WW=0.43), and tended to have lower feed intakes (p=0.052), than those fed on GW. Birds fed on the CMC feeds had significantly inferior FCE than the birds fed the CMC- feeds (days 22–28) (0.44 vs. 0.49). Over the course of the whole infection (days 22–42), birds given feeds containing WW, and those fed on the CMC feeds, had significantly inferior FCE than those fed on the GW, and CMC- feeds (WW=0.49, GW=0.52, CMC =0.50, and CMC-=0.52). Birds fed on the CMC feeds had significantly higher water:feed ratios than those fed on the CMC- feeds throughout the experiment

The RKIP (Raf-1 Kinase Inhibitor Protein) conserved pocket binds to the phosphorylated N-region of Raf-1 and inhibits the Raf-1-mediated activated phosphorylation of MEK

The Raf-MEK-ERK pathway regulates many fundamental biological processes, and its activity is finely tuned at multiple levels. The Raf kinase inhibitory protein (RKIP) is a widely expressed negative modulator of the Raf-MEK-ERK signaling pathway. We have previously shown that RKIP inhibits the phosphorylation of MEK by Raf-1 through interfering with the formation of a kinase-substrate complex by direct binding to both Raf-1 and MEK. Here, we show that the evolutionarily conserved ligand-binding pocket of RKIP is required for its inhibitory activity towards the Raf-1 kinase mediated activation of MEK. Single amino acid substitutions of two of the conserved residues form the base and the wall of the pocket confers a loss-of-function phenotype on RKIP. Loss-of-function RKIP mutants still appear to bind to Raf-1. However the stability of the complexes formed between mutants and the N-region Raf-1 phosphopeptide were drastically reduced. Our results therefore suggest that the RKIP conserved pocket may constitute a novel phosphoamino-acid binding motif and is absolutely required for RKIP function. (C) 2008 Elsevier Inc. All rights reserve

Marc Cassidy, Damien Welch (centre) and Leanne Stojmenov with dancers of the Australian Ballet in Symphonie fantastique by Kryzsztof Pastor in rehearsal for the Destiny season, State Theatre, the Arts Centre, Melbourne, 2007, 9 [picture] /

Title from acquisitions documentation, see file NLA12/324.; Part of the collection: The Australian Ballet in dress rehearsals for the 2007 Destiny season and 2009 Concord season, Melbourne.; Acquired in digital format; access copy available online.; Choreographed by Kryzsztof Pastor.; Destiny evening dress rehearsal 19.08.07.; Second cast.; Mode of access: Online.; Purchased from the photographer, 2012